Mass spectrometric analysis of chondrointin sulfate of bikunin

CARB 72

Lianli Chi, chil@rpi.edu1, Jeremy J Wolff2, Tania Laremore1, I. Jonathan Amster, amster@amstersgi.chem.uga.edu2, and Robert J Linhardt, linhar@rpi.edu3. (1) Department of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, 110 8TH ST, Troy, NY 12180, (2) Department of Chemistry, University of Georgia, Athens, GA 30602, (3) Departments of Chemistry and Chemical Biology, Rensselaer Polytechnic Institute, Center for Biotechnology and Interdisciplinary Studies, 110 8th Street, Troy, NY 12180
Bikunin is a proteoglycan that acts as a trypsin inhibitor in human plasma and can be isolated from urine. A single chondroitin sulfate chain is covalently attached to a core protein in bikunin. The structure and sequence of this chondroitin sulfate chain has not been determined due to its complexity and very high molecular weight. The chondroitin sulfate was released from bikunin and purified. MALDI and FT-ICR MS were performed on the chondroitin sulfate chain. Important structure information of intact chondroitin sulfate chains was obtained. Key words: Mass spectrometry, chondroitin sulfate, bikunin
 

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Division of Carbohydrate Chemistry

The 232nd ACS National Meeting, San Francisco, CA, September 10-14, 2006